Diacylglycerol kinase, catalytic domain
IPR001206
Definition
The DAG-kinase catalytic domain or DAGKc domain is present in mammalian lipid kinases, such as diacylglycerol (DAG), ceramide and sphingosine kinases, as well as in related bacterial proteins [[cite:PMID:8626538], [cite:PMID:17351295]]. Eukaryotic DAG-kinase ([ec:2.7.1.107]) catalyses the phosphorylation of DAG to phosphatidic acid, thus modulating the balance between the two signaling lipids. At least ten different isoforms have been identified in mammals, which form 5 groups characterised by different functional domains, such as the calcium-binding EF hand (see [prositedoc:PDOC00018]), PH (see [prositedoc:PDOC50003]), SAM (see [prositedoc:PDOC50105]) , DAG/PE-binding C1 domain (see [prositedoc:PDOC00379]) and ankyrin repeats (see [prositedoc:PDOC50088]) PMID:17512245.
15 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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